Regulation of myosin phosphatase through phosphorylation of the myosin- binding subunit in platelet activation

Keiji Nakai, Yoshinori Suzuki, Hisakazu Kihira, Hideo Wada, Masanori Fujioka, Masaaki Ito, Takeshi Nakano, Kozo Kaibuchi, Hiroshi Shiku, Masakatsu Nishikawa

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

Human platelets were found to contain myosin phosphatase consisting of a 38-kD catalytic subunit of protein phosphatase type 18, a 130-kD myosin- binding subunit (MBS) and a 20-kD subunit, all of which cross-reacted with antibodies against these subunits of smooth muscle myosin phosphatase. Anti- MBS antibody coimmunoprecipitated RhoA and Rho-kinase of human platelets. Platelets MBS is a substrate for Rho-kinase and phosphorylation of MBS decreases the activity of myosin phosphatase. Treatment of intact platelets with 9,11-epithio-11,12-methano-thromboxane A2 led to a dramatic increase in phosphorylation of MBS and a significant decrease in the activity of myosin phosphatase. These findings suggest a putative mechanism for agonist-induced regulation of myosin phosphatase activity in platelets.

Original languageEnglish
Pages (from-to)3936-3942
Number of pages7
JournalBlood
Volume90
Issue number10
DOIs
Publication statusPublished - 15-11-1997

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Immunology
  • Hematology
  • Cell Biology

Fingerprint Dive into the research topics of 'Regulation of myosin phosphatase through phosphorylation of the myosin- binding subunit in platelet activation'. Together they form a unique fingerprint.

  • Cite this

    Nakai, K., Suzuki, Y., Kihira, H., Wada, H., Fujioka, M., Ito, M., Nakano, T., Kaibuchi, K., Shiku, H., & Nishikawa, M. (1997). Regulation of myosin phosphatase through phosphorylation of the myosin- binding subunit in platelet activation. Blood, 90(10), 3936-3942. https://doi.org/10.1182/blood.v90.10.3936